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Q09013

- DMPK_HUMAN

UniProt

Q09013 - DMPK_HUMAN

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Protein
Myotonin-protein kinase
Gene
DMPK, DM1PK, MDPK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Coiled-coil-mediated oligomerization enhances the catalytic activity. Proteolytic processing of the C-terminus may release the protein from membranes and constitute a mean to regulate the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second messengers.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001ATP
Active sitei195 – 1951Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 859ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. myosin phosphatase regulator activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular calcium ion homeostasis Source: UniProtKB
  2. muscle cell apoptotic process Source: UniProtKB
  3. nuclear envelope organization Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. regulation of catalytic activity Source: GOC
  6. regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction Source: Ensembl
  7. regulation of heart contraction Source: UniProtKB
  8. regulation of myotube differentiation Source: UniProtKB
  9. regulation of skeletal muscle contraction by calcium ion signaling Source: Ensembl
  10. regulation of sodium ion transport Source: Ensembl
  11. regulation of synapse structural plasticity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiQ09013.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotonin-protein kinase (EC:2.7.11.1)
Short name:
MT-PK
Alternative name(s):
DM-kinase
Short name:
DMK
DM1 protein kinase
DMPK
Myotonic dystrophy protein kinase
Gene namesi
Name:DMPK
Synonyms:DM1PK, MDPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2933. DMPK.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side By similarity. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Inferred. Mitochondrion outer membrane; Single-pass type IV membrane protein Inferred. Sarcoplasmic reticulum membrane By similarity. Cell membrane By similarity. Cytoplasmcytosol By similarity
Note: Localizes to sarcoplasmic reticulum membranes of cardiomyocytes By similarity.3 Publications
Isoform 1 : Mitochondrion membrane 3 Publications
Isoform 3 : Mitochondrion membrane 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 590590Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei591 – 61121Helical; Anchor for type IV membrane protein; Reviewed prediction
Add
BLAST
Topological domaini612 – 62918Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of mitochondrial outer membrane Source: UniProtKB
  4. nuclear membrane Source: UniProtKB
  5. nuclear outer membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB
  7. sarcoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias.
Note: The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001K → A: Loss of kinase activity. 1 Publication

Keywords - Diseasei

Cataract

Organism-specific databases

MIMi160900. phenotype.
Orphaneti273. Steinert myotonic dystrophy.
PharmGKBiPA27380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Myotonin-protein kinase
PRO_0000085924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161Phosphoserine; by autocatalysis By similarity
Modified residuei228 – 2281Phosphoserine; by autocatalysis By similarity
Modified residuei234 – 2341Phosphothreonine; by autocatalysis By similarity

Post-translational modificationi

Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK.1 Publication
Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ09013.
PRIDEiQ09013.

2D gel databases

REPRODUCTION-2DPAGEQ09013.

PTM databases

PhosphoSiteiQ09013.

Expressioni

Tissue specificityi

Most isoforms are expressed in many tissues including heart, skeletal muscle, liver and brain, except for isoform 2 which is only found in the heart and skeletal muscle, and isoform 14 which is only found in the brain, with high levels in the striatum, cerebellar cortex and pons.1 Publication

Gene expression databases

ArrayExpressiQ09013.
BgeeiQ09013.
CleanExiHS_DMPK.
GenevestigatoriQ09013.

Organism-specific databases

HPAiHPA007164.
HPA008905.

Interactioni

Subunit structurei

Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PLNP266784EBI-692774,EBI-692836

Protein-protein interaction databases

BioGridi108100. 15 interactions.
IntActiQ09013. 15 interactions.
MINTiMINT-195910.
STRINGi9606.ENSP00000345997.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154
Turni17 – 193
Helixi22 – 3716
Helixi40 – 434
Helixi45 – 6420
Helixi68 – 703
Beta strandi71 – 799
Beta strandi84 – 907
Turni91 – 933
Beta strandi96 – 1038
Helixi104 – 1107
Helixi111 – 1133
Helixi116 – 12510
Turni128 – 1303
Beta strandi134 – 1396
Beta strandi141 – 1488
Helixi156 – 1638
Helixi169 – 18820
Helixi198 – 2003
Beta strandi201 – 2033
Beta strandi209 – 2113
Helixi235 – 2373
Helixi240 – 2478
Beta strandi253 – 2553
Helixi258 – 27316
Helixi283 – 2919
Helixi293 – 2964
Helixi308 – 3158
Helixi321 – 3233
Turni325 – 3295
Helixi330 – 3345
Helixi337 – 3393
Beta strandi378 – 3825
Turni385 – 3873
Helixi398 – 4003
Helixi412 – 4143
Helixi468 – 52861

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WT6X-ray1.60A/B/D460-537[»]
2VD5X-ray2.80A/B11-420[»]
ProteinModelPortaliQ09013.
SMRiQ09013. Positions 11-416, 461-527.

Miscellaneous databases

EvolutionaryTraceiQ09013.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 339269Protein kinase
Add
BLAST
Domaini340 – 41576AGC-kinase C-terminal
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili457 – 536802 Publications
Add
BLAST

Domaini

The coiled coil domain is required for homodimerization and regulates the enzymatic activity.2 Publications

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG107817.
KOiK08788.
OMAiTHCNISS.
OrthoDBiEOG7F511X.
TreeFamiTF105337.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q09013-9) [UniParc]FASTAAdd to Basket

Also known as: DMPK A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF    50
LQWAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK 100
IMNKWDMLKR GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY 150
YVGGDLLTLL SKFGERIPAE MARFYLAEIV MAIDSVHRLG YVHRDIKPDN 200
ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP EILQAVGGGP 250
GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 300
LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 350
VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF 400
VGYSYSCMAL RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE 450
VAVPAAVPAA EAEAEVTLRE LQEALEEEVL TRQSLSREME AIRTDNQNFA 500
SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS PRATDPPSHL 550
DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS LLLFAVVLSR 600
AAALGCIGLV AHAGQLTAVW RRPGAARAP 629
Length:629
Mass (Da):69,385
Last modified:December 14, 2011 - v3
Checksum:i46783ED4AE65B493
GO
Isoform 2 (identifier: Q09013-11) [UniParc]FASTAAdd to Basket

Also known as: DMPK B

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.

Show »
Length:624
Mass (Da):69,028
Checksum:i7ECA31ED9A84E7E1
GO
Isoform 3 (identifier: Q09013-16) [UniParc]FASTAAdd to Basket

Also known as: DMPK C

The sequence of this isoform differs from the canonical sequence as follows:
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

Note: No experimental confirmation available.

Show »
Length:630
Mass (Da):69,950
Checksum:i52B2B388CD99AA2F
GO
Isoform 4 (identifier: Q09013-15) [UniParc]FASTAAdd to Basket

Also known as: DMPK D

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

Show »
Length:625
Mass (Da):69,592
Checksum:i10EA0187F4AD4B7C
GO
Isoform 5 (identifier: Q09013-10) [UniParc]FASTAAdd to Basket

Also known as: DMPK E

The sequence of this isoform differs from the canonical sequence as follows:
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Show »
Length:535
Mass (Da):59,804
Checksum:i9A08CEA02FAE8828
GO
Isoform 6 (identifier: Q09013-12) [UniParc]FASTAAdd to Basket

Also known as: DMPK F

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Show »
Length:530
Mass (Da):59,446
Checksum:i5E41498FDA6C22D4
GO
Isoform 7 (identifier: Q09013-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP

Show »
Length:639
Mass (Da):70,371
Checksum:i69A831604F7F8D38
GO
Isoform 8 (identifier: Q09013-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: No experimental confirmation available.

Show »
Length:540
Mass (Da):59,334
Checksum:iA7BB715CB845055C
GO
Isoform 9 (identifier: Q09013-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     226-275: Missing.

Note: No experimental confirmation available.

Show »
Length:589
Mass (Da):65,076
Checksum:i2558F658CFA1FCE1
GO
Isoform 10 (identifier: Q09013-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     378-382: Missing.

Note: No experimental confirmation available.

Show »
Length:634
Mass (Da):70,014
Checksum:i94F39ADE9A8F4AFC
GO
Isoform 11 (identifier: Q09013-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     550-579: Missing.

Note: No experimental confirmation available.

Show »
Length:609
Mass (Da):67,263
Checksum:i58A97059F9590719
GO
Isoform 12 (identifier: Q09013-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Show »
Length:545
Mass (Da):60,790
Checksum:iEF016FDBE3933553
GO

Sequence cautioni

The sequence AAA87583.1 differs from that shown. Reason: Probable cloning artifact.
The sequence AAA64884.1 differs from that shown. Reason: Frameshift at positions 56, 555 and 568.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti423 – 4231L → V.4 Publications
Corresponds to variant rs527221 [ dbSNP | Ensembl ].
VAR_058334
Natural varianti428 – 4281L → V in a lung small cell carcinoma sample; somatic mutation. 1 Publication
VAR_040452

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 8.
VSP_042098Add
BLAST
Alternative sequencei1 – 5353MSAEV…DFLQW → MGGHFWPPEPYTVFMWGSPW EADSPRVKLRGREKGRQTEG GAFPLVSSALSGDPRFFSPT TPP in isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12.
VSP_042099Add
BLAST
Alternative sequencei226 – 27550Missing in isoform 9.
VSP_042100Add
BLAST
Alternative sequencei378 – 3825Missing in isoform 2, isoform 4, isoform 6 and isoform 10.
VSP_042101
Alternative sequencei534 – 5352AV → GP in isoform 5, isoform 6 and isoform 12.
VSP_042102
Alternative sequencei536 – 62994Missing in isoform 5, isoform 6 and isoform 12.
VSP_042103Add
BLAST
Alternative sequencei550 – 62980LDGPP…AARAP → MAPRPWLWASARWWGQAPCT AATCCSLPGSLGLAYRRRFP CSCSPLFCLVPPPWAALGWW PTPANSPQSGAAQEPPALPE P in isoform 3 and isoform 4.
VSP_042104Add
BLAST
Alternative sequencei550 – 57930Missing in isoform 11.
VSP_042105Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti474 – 4741A → P in AAB31800. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87312 mRNA. No translation available.
L19268 mRNA. Translation: AAA36206.1.
L19266 Genomic DNA. Translation: AAA36205.1.
L08835 Genomic DNA. Translation: AAC14449.1.
L08835 Genomic DNA. Translation: AAC14451.1.
L08835 Genomic DNA. Translation: AAC14448.1.
L08835 Genomic DNA. Translation: AAC14450.1.
L00727 Genomic DNA. Translation: AAA75235.1.
L00727 Genomic DNA. Translation: AAA75236.1.
L00727 Genomic DNA. Translation: AAA75237.1.
L00727 Genomic DNA. Translation: AAA75238.1.
L00727 Genomic DNA. Translation: AAA75239.1.
L00727 Genomic DNA. Translation: AAA75240.1.
S72883 mRNA. Translation: AAB31800.1.
HQ205626 Genomic DNA. Translation: ADP91337.1.
HQ205627 Genomic DNA. Translation: ADP91341.1.
HQ205628 Genomic DNA. Translation: ADP91345.1.
HQ205629 Genomic DNA. Translation: ADP91349.1.
HQ205630 Genomic DNA. Translation: ADP91353.1.
HQ205631 Genomic DNA. Translation: ADP91357.1.
HQ205632 Genomic DNA. Translation: ADP91361.1.
HQ205633 Genomic DNA. Translation: ADP91365.1.
HQ205634 Genomic DNA. Translation: ADP91369.1.
HQ205635 Genomic DNA. Translation: ADP91373.1.
HQ205636 Genomic DNA. Translation: ADP91377.1.
HQ205637 Genomic DNA. Translation: ADP91381.1.
HQ205638 Genomic DNA. Translation: ADP91385.1.
HQ205639 Genomic DNA. Translation: ADP91389.1.
HQ205640 Genomic DNA. Translation: ADP91393.1.
HQ205641 Genomic DNA. Translation: ADP91397.1.
HQ205642 Genomic DNA. Translation: ADP91401.1.
HQ205643 Genomic DNA. Translation: ADP91405.1.
HQ205644 Genomic DNA. Translation: ADP91409.1.
HQ205645 Genomic DNA. Translation: ADP91413.1.
HQ205646 Genomic DNA. Translation: ADP91417.1.
HQ205647 Genomic DNA. Translation: ADP91421.1.
HQ205648 Genomic DNA. Translation: ADP91425.1.
HQ205649 Genomic DNA. Translation: ADP91429.1.
HQ205650 Genomic DNA. Translation: ADP91433.1.
HQ205651 Genomic DNA. Translation: ADP91437.1.
HQ205652 Genomic DNA. Translation: ADP91441.1.
HQ205653 Genomic DNA. Translation: ADP91445.1.
HQ205654 Genomic DNA. Translation: ADP91449.1.
HQ205655 Genomic DNA. Translation: ADP91453.1.
HQ205656 Genomic DNA. Translation: ADP91457.1.
HQ205657 Genomic DNA. Translation: ADP91461.1.
HQ205658 Genomic DNA. Translation: ADP91465.1.
HQ205659 Genomic DNA. Translation: ADP91469.1.
HQ205660 Genomic DNA. Translation: ADP91473.1.
HQ205661 Genomic DNA. Translation: ADP91477.1.
HQ205662 Genomic DNA. Translation: ADP91481.1.
HQ205663 Genomic DNA. Translation: ADP91485.1.
HQ205664 Genomic DNA. Translation: ADP91489.1.
HQ205665 Genomic DNA. Translation: ADP91493.1.
KJ534827 mRNA. Translation: AHW56467.1.
CH471126 Genomic DNA. Translation: EAW57380.1.
CH471126 Genomic DNA. Translation: EAW57382.1.
BC062553 mRNA. Translation: AAH62553.1.
M94203 mRNA. Translation: AAA64884.1. Frameshift.
U46546 mRNA. Translation: AAA87583.1. Sequence problems.
CCDSiCCDS12674.1. [Q09013-9]
CCDS46117.1. [Q09013-15]
CCDS46118.1. [Q09013-11]
CCDS46119.1. [Q09013-1]
PIRiB49364.
RefSeqiNP_001075029.1. NM_001081560.2. [Q09013-11]
NP_001075031.1. NM_001081562.2. [Q09013-15]
NP_001075032.1. NM_001081563.2. [Q09013-1]
NP_001275694.1. NM_001288765.1.
NP_004400.4. NM_004409.4. [Q09013-9]
UniGeneiHs.631596.

Genome annotation databases

EnsembliENST00000291270; ENSP00000291270; ENSG00000104936. [Q09013-9]
ENST00000343373; ENSP00000345997; ENSG00000104936. [Q09013-1]
ENST00000354227; ENSP00000346168; ENSG00000104936. [Q09013-12]
ENST00000447742; ENSP00000413417; ENSG00000104936. [Q09013-11]
ENST00000458663; ENSP00000401753; ENSG00000104936. [Q09013-15]
GeneIDi1760.
KEGGihsa:1760.
UCSCiuc002pdf.1. human. [Q09013-9]
uc010xxs.1. human. [Q09013-16]
uc010xxt.1. human. [Q09013-12]

Polymorphism databases

DMDMi363548519.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87312 mRNA. No translation available.
L19268 mRNA. Translation: AAA36206.1 .
L19266 Genomic DNA. Translation: AAA36205.1 .
L08835 Genomic DNA. Translation: AAC14449.1 .
L08835 Genomic DNA. Translation: AAC14451.1 .
L08835 Genomic DNA. Translation: AAC14448.1 .
L08835 Genomic DNA. Translation: AAC14450.1 .
L00727 Genomic DNA. Translation: AAA75235.1 .
L00727 Genomic DNA. Translation: AAA75236.1 .
L00727 Genomic DNA. Translation: AAA75237.1 .
L00727 Genomic DNA. Translation: AAA75238.1 .
L00727 Genomic DNA. Translation: AAA75239.1 .
L00727 Genomic DNA. Translation: AAA75240.1 .
S72883 mRNA. Translation: AAB31800.1 .
HQ205626 Genomic DNA. Translation: ADP91337.1 .
HQ205627 Genomic DNA. Translation: ADP91341.1 .
HQ205628 Genomic DNA. Translation: ADP91345.1 .
HQ205629 Genomic DNA. Translation: ADP91349.1 .
HQ205630 Genomic DNA. Translation: ADP91353.1 .
HQ205631 Genomic DNA. Translation: ADP91357.1 .
HQ205632 Genomic DNA. Translation: ADP91361.1 .
HQ205633 Genomic DNA. Translation: ADP91365.1 .
HQ205634 Genomic DNA. Translation: ADP91369.1 .
HQ205635 Genomic DNA. Translation: ADP91373.1 .
HQ205636 Genomic DNA. Translation: ADP91377.1 .
HQ205637 Genomic DNA. Translation: ADP91381.1 .
HQ205638 Genomic DNA. Translation: ADP91385.1 .
HQ205639 Genomic DNA. Translation: ADP91389.1 .
HQ205640 Genomic DNA. Translation: ADP91393.1 .
HQ205641 Genomic DNA. Translation: ADP91397.1 .
HQ205642 Genomic DNA. Translation: ADP91401.1 .
HQ205643 Genomic DNA. Translation: ADP91405.1 .
HQ205644 Genomic DNA. Translation: ADP91409.1 .
HQ205645 Genomic DNA. Translation: ADP91413.1 .
HQ205646 Genomic DNA. Translation: ADP91417.1 .
HQ205647 Genomic DNA. Translation: ADP91421.1 .
HQ205648 Genomic DNA. Translation: ADP91425.1 .
HQ205649 Genomic DNA. Translation: ADP91429.1 .
HQ205650 Genomic DNA. Translation: ADP91433.1 .
HQ205651 Genomic DNA. Translation: ADP91437.1 .
HQ205652 Genomic DNA. Translation: ADP91441.1 .
HQ205653 Genomic DNA. Translation: ADP91445.1 .
HQ205654 Genomic DNA. Translation: ADP91449.1 .
HQ205655 Genomic DNA. Translation: ADP91453.1 .
HQ205656 Genomic DNA. Translation: ADP91457.1 .
HQ205657 Genomic DNA. Translation: ADP91461.1 .
HQ205658 Genomic DNA. Translation: ADP91465.1 .
HQ205659 Genomic DNA. Translation: ADP91469.1 .
HQ205660 Genomic DNA. Translation: ADP91473.1 .
HQ205661 Genomic DNA. Translation: ADP91477.1 .
HQ205662 Genomic DNA. Translation: ADP91481.1 .
HQ205663 Genomic DNA. Translation: ADP91485.1 .
HQ205664 Genomic DNA. Translation: ADP91489.1 .
HQ205665 Genomic DNA. Translation: ADP91493.1 .
KJ534827 mRNA. Translation: AHW56467.1 .
CH471126 Genomic DNA. Translation: EAW57380.1 .
CH471126 Genomic DNA. Translation: EAW57382.1 .
BC062553 mRNA. Translation: AAH62553.1 .
M94203 mRNA. Translation: AAA64884.1 . Frameshift.
U46546 mRNA. Translation: AAA87583.1 . Sequence problems.
CCDSi CCDS12674.1. [Q09013-9 ]
CCDS46117.1. [Q09013-15 ]
CCDS46118.1. [Q09013-11 ]
CCDS46119.1. [Q09013-1 ]
PIRi B49364.
RefSeqi NP_001075029.1. NM_001081560.2. [Q09013-11 ]
NP_001075031.1. NM_001081562.2. [Q09013-15 ]
NP_001075032.1. NM_001081563.2. [Q09013-1 ]
NP_001275694.1. NM_001288765.1.
NP_004400.4. NM_004409.4. [Q09013-9 ]
UniGenei Hs.631596.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WT6 X-ray 1.60 A/B/D 460-537 [» ]
2VD5 X-ray 2.80 A/B 11-420 [» ]
ProteinModelPortali Q09013.
SMRi Q09013. Positions 11-416, 461-527.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108100. 15 interactions.
IntActi Q09013. 15 interactions.
MINTi MINT-195910.
STRINGi 9606.ENSP00000345997.

Chemistry

BindingDBi Q09013.
ChEMBLi CHEMBL5320.
GuidetoPHARMACOLOGYi 1505.

PTM databases

PhosphoSitei Q09013.

Polymorphism databases

DMDMi 363548519.

2D gel databases

REPRODUCTION-2DPAGE Q09013.

Proteomic databases

PaxDbi Q09013.
PRIDEi Q09013.

Protocols and materials databases

DNASUi 1760.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000291270 ; ENSP00000291270 ; ENSG00000104936 . [Q09013-9 ]
ENST00000343373 ; ENSP00000345997 ; ENSG00000104936 . [Q09013-1 ]
ENST00000354227 ; ENSP00000346168 ; ENSG00000104936 . [Q09013-12 ]
ENST00000447742 ; ENSP00000413417 ; ENSG00000104936 . [Q09013-11 ]
ENST00000458663 ; ENSP00000401753 ; ENSG00000104936 . [Q09013-15 ]
GeneIDi 1760.
KEGGi hsa:1760.
UCSCi uc002pdf.1. human. [Q09013-9 ]
uc010xxs.1. human. [Q09013-16 ]
uc010xxt.1. human. [Q09013-12 ]

Organism-specific databases

CTDi 1760.
GeneCardsi GC19M046272.
GeneReviewsi DMPK.
H-InvDB HIX0137522.
HGNCi HGNC:2933. DMPK.
HPAi HPA007164.
HPA008905.
MIMi 160900. phenotype.
605377. gene.
neXtProti NX_Q09013.
Orphaneti 273. Steinert myotonic dystrophy.
PharmGKBi PA27380.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG107817.
KOi K08788.
OMAi THCNISS.
OrthoDBi EOG7F511X.
TreeFami TF105337.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
SignaLinki Q09013.

Miscellaneous databases

ChiTaRSi DMPK. human.
EvolutionaryTracei Q09013.
GeneWikii Myotonin-protein_kinase.
GenomeRNAii 1760.
NextBioi 7169.
PROi Q09013.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q09013.
Bgeei Q09013.
CleanExi HS_DMPK.
Genevestigatori Q09013.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
ProDomi PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), INVOLVEMENT IN DM1.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT VAL-423.
    Tissue: Brain and Muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 5; 6), VARIANT VAL-423.
  4. "Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy."
    Fu Y.-H., Friedman D.L., Richards S., Pearlman J.A., Gibbs R.A., Pizzuti A., Ashizawa T., Perryman M.B., Scarlato G., Fenwick R.G. Jr., Caskey C.T.
    Science 260:235-238(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 7; 8; 9; 10; 11 AND 12), VARIANT VAL-423.
  5. "Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells."
    Sasagawa N., Sorimachi H., Maruyama K., Arahata K., Ishiura S., Suzuki K.
    FEBS Lett. 351:22-26(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Muscle.
  6. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
    Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
    Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7).
  7. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
    Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
    , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
    Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
    Tissue: Fetal brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Prostate.
  10. "Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member."
    Brook J.D., McCurrach M., Harley H.G., Buckler A.J., Church D., Aburatani H., Hunter K., Stanton V.P., Thirion J.-P., Hudson T., Sohn R., Zemelman B., Snell R.G., Rundle S.A., Crow S., Davies J., Shelbourne P., Buxton J.
    , Jones C., Juvonen V., Johnson K., Harper P.S., Shaw D.J., Housman D.E.
    Cell 68:799-808(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-629 (ISOFORM 2), INVOLVEMENT IN DM1, VARIANT VAL-423.
  11. "Different expression of the myotonin protein kinase gene in discrete areas of human brain."
    Gennarelli M., Lucarelli M., Zelano G., Pizzuti A., Novelli G., Dallapiccola B.
    Biochem. Biophys. Res. Commun. 216:489-494(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-619 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  12. Cited for: ALTERNATIVE SPLICING, INVOLVEMENT IN DM1.
    Tissue: Brain and Heart.
  13. "MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase."
    Suzuki A., Sugiyama Y., Hayashi Y., Nyu-i N., Yoshida M., Nonaka I., Ishiura S., Arahata K., Ohno S.
    J. Cell Biol. 140:1113-1124(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPB2, ENZYME REGULATION.
    Tissue: Muscle.
  14. "Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition."
    Bush E.W., Helmke S.M., Birnbaum R.A., Perryman M.B.
    Biochemistry 39:8480-8490(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  15. "Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase."
    Shimizu M., Wang W., Walch E.T., Dunne P.W., Epstein H.F.
    FEBS Lett. 475:273-277(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAC1, PHOSPHORYLATION BY RAF1, ENZYME REGULATION.
  16. "Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties."
    Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G., Wieringa B.
    Hum. Mol. Genet. 9:605-616(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6).
  17. Cited for: FUNCTION IN PHOSPHORYLATION OF FXYD1/PLM.
  18. "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
    Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
    FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
  19. "Homodimerization through coiled-coil regions enhances activity of the myotonic dystrophy protein kinase."
    Zhang R., Epstein H.F.
    FEBS Lett. 546:281-287(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, ENZYME REGULATION.
  20. "Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum."
    Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.
    J. Biol. Chem. 280:8016-8021(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PLN, MUTAGENESIS OF LYS-100, INTERACTION WITH PLN.
  21. "Divergent mitochondrial and endoplasmic reticulum association of DMPK splice isoforms depends on unique sequence arrangements in tail anchors."
    van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B., van de Loo F.A., Fransen J., Wieringa B., Wansink D.G.
    Mol. Cell. Biol. 25:1402-1414(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
  22. Cited for: INVOLVEMENT IN DM1.
  23. "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
    Tan I., Lai J., Yong J., Li S.F., Leung T.
    FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
  24. "Myotonic dystrophy protein kinase is critical for nuclear envelope integrity."
    Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B.
    J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEAR ENVELOPE STABILITY, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
  25. "Crystallization and preliminary X-ray analysis of the coiled-coil domain of dystrophia myotonica kinase."
    Garcia P., Marino M., Mayans O.
    Acta Crystallogr. D 60:2336-2339(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, COILED-COIL DOMAIN.
  26. "Molecular insights into the self-assembly mechanism of dystrophia myotonica kinase."
    Garcia P., Ucurum Z., Bucher R., Svergun D.I., Huber T., Lustig A., Konarev P.V., Marino M., Mayans O.
    FASEB J. 20:1142-1151(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, SUBUNIT, COILED-COIL DOMAIN.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-430 IN COMPLEX WITH INHIBITOR BIM-8, SUBUNIT.
  28. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-428.

Entry informationi

Entry nameiDMPK_HUMAN
AccessioniPrimary (citable) accession number: Q09013
Secondary accession number(s): E5KR08, Q16205, Q6P5Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 14, 2011
Last modified: September 3, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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